Recombinant Human RPL18A protein (denatured) (His tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

RPL18A also known as 60S ribosomal protein L18a plays a part in ribosome structure and function. This ribosomal protein with a molecular mass of approximately 22 kDa is an important part of the large 60S subunit of the ribosome. It is present in various tissues and has ubiquitous expression reflecting its role in protein synthesis. It functions as a structural constituent and it interacts directly with ribosomal RNA to help create the core framework necessary for ribosome stability.

Biological function summary

Ribosomal protein L18a contributes to the assembly and function of ribosomes the essential machines for translation of mRNA into proteins. It is a part of the ribosomal complex which includes numerous proteins and RNA molecules that collaborate for translation. L18a assists in maintaining the proper structure needed for the translation process impacting cell growth and proliferation. Also ribosomal proteins like RPL18A have non-ribosomal roles in regulating cell cycle and apoptosis showing their importance beyond protein synthesis.

Pathways

Ribosome biogenesis and protein synthesis involve RPL18A. It is a component of the ribosomal pathway closely related to other ribosomal proteins like RPL5 and RPL11 essential for the synthesis of new proteins. RPL18A also intersects with the mTOR signaling pathway which senses nutritional and energy conditions to regulate cell growth emphasizing its role in metabolic control.

Mutations or dysregulation of RPL18A connect to conditions such as Diamond-Blackfan anemia a rare genetic disorder resulting in failure to make red blood cells. RPL18A mutation leads to disrupted ribosome biogenesis similarly observed in many cancers where rapid cell growth demands increased protein synthesis. The interaction between RPL18A and other ribosomal proteins like RPL11 suggests their combined influence on the progression of these disorders by altering ribosomal function and cellular homeostasis.